NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|215694735|dbj|BAG89926|]
View 

unnamed protein product [Oryza sativa Japonica Group]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10085251)

cyclophilin-type peptidylprolyl isomerase catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins

CATH:  2.40.100.10
EC:  5.2.1.8
Gene Ontology:  GO:0006457|GO:0003755|GO:0000413
PubMed:  14731520|15998457|15353287

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 82-226 2.96e-48

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.


:

Pssm-ID: 238194 [Multi-domain]  Cd Length: 146  Bit Score: 155.50  E-value: 2.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  82 VIDTAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAAQeWILKAKASGENALSPKH-E 160
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHhR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215694735 161 AFMIGTTKNPNNK-GFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYQPKTPIGILN 226
Cdd:cd00317   80 RGTLSMANAGPNTnGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
 
Name Accession Description Interval E-value
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 82-226 2.96e-48

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.


Pssm-ID: 238194 [Multi-domain]  Cd Length: 146  Bit Score: 155.50  E-value: 2.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  82 VIDTAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAAQeWILKAKASGENALSPKH-E 160
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHhR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215694735 161 AFMIGTTKNPNNK-GFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYQPKTPIGILN 226
Cdd:cd00317   80 RGTLSMANAGPNTnGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 80-231 5.80e-34

Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 119.50  E-value: 5.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  80 YAVIDTAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAaqewilkaKASG-----ENA 154
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGT--------GGPGytipdEFD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215694735 155 LSPKHEAFMIG--TTKNPNNKGFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYQPKTPIGILNITLKQ 231
Cdd:COG0652   80 PGLKHKRGTLAmaRAQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTIVE 158
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 87-228 3.11e-30

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 109.65  E-value: 3.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735   87 KGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAAQEWILKAKASgENALSPKHEAFMIG- 165
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDE-IFPLLLKHKRGALSm 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215694735  166 --TTKNPNNKGFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEhYQPKTPIGILNIT 228
Cdd:pfam00160  85 anTGPAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCG 148
PTZ00060 PTZ00060
cyclophilin; Provisional
 83-226 4.28e-23

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 92.22  E-value: 4.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  83 IDTAK-GSITIEIYKDASADVVDRFVSLC---------KSNHFKGMPFRHVIKNFVIQGGDF-DFNGAAQEWILKAKASG 151
Cdd:PTZ00060  24 IDNAPaGRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDItNHNGTGGESIYGRKFTD 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215694735 152 ENaLSPKHEAFMIGTTKN--PNNKGFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYqPKTPIGILN 226
Cdd:PTZ00060 104 EN-FKLKHDQPGLLSMANagPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGY-PKKPVVVTD 178
 
Name Accession Description Interval E-value
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 82-226 2.96e-48

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.


Pssm-ID: 238194 [Multi-domain]  Cd Length: 146  Bit Score: 155.50  E-value: 2.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  82 VIDTAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAAQeWILKAKASGENALSPKH-E 160
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHhR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215694735 161 AFMIGTTKNPNNK-GFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYQPKTPIGILN 226
Cdd:cd00317   80 RGTLSMANAGPNTnGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 80-231 5.80e-34

Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 119.50  E-value: 5.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  80 YAVIDTAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAaqewilkaKASG-----ENA 154
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGT--------GGPGytipdEFD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215694735 155 LSPKHEAFMIG--TTKNPNNKGFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYQPKTPIGILNITLKQ 231
Cdd:COG0652   80 PGLKHKRGTLAmaRAQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTIVE 158
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 87-228 3.11e-30

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 109.65  E-value: 3.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735   87 KGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAAQEWILKAKASgENALSPKHEAFMIG- 165
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDE-IFPLLLKHKRGALSm 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215694735  166 --TTKNPNNKGFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEhYQPKTPIGILNIT 228
Cdd:pfam00160  85 anTGPAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCG 148
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 88-224 6.27e-26

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.


Pssm-ID: 238907 [Multi-domain]  Cd Length: 164  Bit Score: 98.87  E-value: 6.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  88 GSITIEIYKDASADVVDRFVSLC--------KSNHFKGMPFRHVIKNFVIQGGDF-DFNGAAQEWILKAKASGENaLSPK 158
Cdd:cd01926   15 GRIVMELFADVVPKTAENFRALCtgekgkggKPFGYKGSTFHRVIPDFMIQGGDFtRGNGTGGKSIYGEKFPDEN-FKLK 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215694735 159 HEAFMIGTTKN--PNNKGFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDeHYQPKTPIGI 224
Cdd:cd01926   94 HTGPGLLSMANagPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKKKVVI 160
PTZ00060 PTZ00060
cyclophilin; Provisional
 83-226 4.28e-23

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 92.22  E-value: 4.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  83 IDTAK-GSITIEIYKDASADVVDRFVSLC---------KSNHFKGMPFRHVIKNFVIQGGDF-DFNGAAQEWILKAKASG 151
Cdd:PTZ00060  24 IDNAPaGRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDItNHNGTGGESIYGRKFTD 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215694735 152 ENaLSPKHEAFMIGTTKN--PNNKGFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYqPKTPIGILN 226
Cdd:PTZ00060 104 EN-FKLKHDQPGLLSMANagPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGY-PKKPVVVTD 178
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 82-229 1.48e-22

Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a histidine at this position. The exact function of the protein is not known.


Pssm-ID: 238909 [Multi-domain]  Cd Length: 153  Bit Score: 89.80  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  82 VIDTAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAAQEWILKAKASGENALSPKHEA 161
Cdd:cd01928    4 TLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHDS 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735 162 FMIGTTKN--PNNKGFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYQPKTPIGILNITL 229
Cdd:cd01928   84 RGVVSMANngPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKDVTI 153
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 80-229 6.30e-22

cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination.


Pssm-ID: 238904 [Multi-domain]  Cd Length: 159  Bit Score: 88.24  E-value: 6.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  80 YAVIDTAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAAQEWILKAKASGENALSPKH 159
Cdd:cd01923    1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215694735 160 EAFMIGTTKN--PNNKGFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYQPKTPIGILNITL 229
Cdd:cd01923   81 DGRGVLSMANsgPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTSV 152
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 43-224 1.29e-17

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 77.57  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  43 ATYRHWHHRPmletemdlPRAEHVGRSEDSTKTSRPSyavidtakGSITIEIYKDASADVVDRFVSLCKSNH-------- 114
Cdd:PLN03149   4 AGNVEWHLRP--------PNPKNPVVFFDVTIGGIPA--------GRIKMELFADIAPKTAENFRQFCTGEFrkaglpqg 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735 115 FKGMPFRHVIKNFVIQGGDF---DFNGAAQewILKAKASGENALSpKHEAFMIGTTKN--PNNKGFDLFITTAPIPDLND 189
Cdd:PLN03149  68 YKGCQFHRVIKDFMIQGGDFlkgDGTGCVS--IYGSKFEDENFIA-KHTGPGLLSMANsgPNTNGCQFFITCAKCDWLDN 144

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 215694735 190 KLVVFGQVI-NGQDIVQEIEEVDTDEHYQPKTPIGI 224
Cdd:PLN03149 145 KHVVFGRVLgDGLLVVRKIENVATGPNNRPKLACVI 180
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 82-224 2.25e-14

cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a C-terminal RNA recognition motif domain (RRM). This subfamily of the cyclophilin domain family contains a number of eukaryotic cyclophilins having the RRM domain including the nuclear proteins: human hCyP-57, Arabidopsis thaliana AtCYP59, Caenorhabditis elegans CeCyP-44 and Paramecium tetrurelia Kin241. The Kin241 protein has been shown to have a role in cell morphogenesis.


Pssm-ID: 238902 [Multi-domain]  Cd Length: 166  Bit Score: 68.52  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  82 VIDTAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAAQEWILKaKASGENA------L 155
Cdd:cd01921    1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYS-QLYGRQArffepeI 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215694735 156 SPKHEAFMIGT----TKNPNNKGFDLFITTAP-IPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYQPKTPIGI 224
Cdd:cd01921   80 LPLLKHSKKGTvsmvNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 83-224 7.05e-14

cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to the cytosolic E. coli cyclophilin A and Streptomyces antibioticus SanCyp18. Compared to the archetypal cyclophilin Human cyclophilin A, these have reduced affinity for cyclosporin A. E. coli cyclophilin A has a similar peptidylprolyl cis- trans isomerase activity to the human cyclophilin A. Most members of this subfamily contain a phenylalanine residue at the position equivalent to Human cyclophilin W121, where a tyrptophan has been shown to be important for cyclophilin binding.


Pssm-ID: 238901 [Multi-domain]  Cd Length: 155  Bit Score: 66.70  E-value: 7.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  83 IDTAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFDFNGAAQEWILKAKASGENALSPKHEAF 162
Cdd:cd01920    2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGTI 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215694735 163 MIGTTKNPNNKGFDLFITTAPIPDLNDK-----LVVFGQVINGQDIVQEIEEVDTDEH--YQ--PKTPIGI 224
Cdd:cd01920   82 AMARTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETYSFgsYQdvPVQDVII 152
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 85-212 5.26e-09

cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation.


Pssm-ID: 238905  Cd Length: 176  Bit Score: 53.99  E-value: 5.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  85 TAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGD-----FDF----NGAAQEWILKAKASG---- 151
Cdd:cd01924    4 TDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDpqgknPGFpdpeTGKSRTIPLEIKPEGqkqp 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735 152 -------------ENALSPKHEAFMIGT--TKNPNNKG--------FDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIE 208
Cdd:cd01924   84 vygktleeagrydEQPVLPFNAFGAIAMarTEFDPNSAssqfffllKDNELTPSRNNVLDGRYAVFGYVTDGLDILRELK 163


                 ....
gi 215694735 209 EVDT 212
Cdd:cd01924  164 VGDK 167
PRK10903 PRK10903
peptidylprolyl isomerase A;
79-226 2.44e-08

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 52.15  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215694735  79 SYAVIDTAKGSITIEIYKDASADVVDRFVSLCKSNHFKGMPFRHVIKNFVIQGGDFdfNGAAQEWILKA--KASGENALS 156
Cdd:PRK10903  29 PHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGF--TEQMQQKKPNPpiKNEADNGLR 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215694735 157 PKHEAFMIGTTKNPNNKGFDLFITTAPIPDLNDK-----LVVFGQVINGQDIVQEIEEVDTDE--HYQ--PKTPIGILN 226
Cdd:PRK10903 107 NTRGTIAMARTADKDSATSQFFINVADNAFLDHGqrdfgYAVFGKVVKGMDVADKISQVPTHDvgPYQnvPSKPVVILS 185
PTZ00221 PTZ00221
cyclophilin; Provisional
 166-224 1.70e-04

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 41.78  E-value: 1.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 215694735 166 TTKNPNNKGFDLFITTAPIPDLNDKLVVFGQVINGQDIVQEIEEVDTDEHYQPKTPIGI 224
Cdd:PTZ00221 155 ISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPLLPVTV 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH